1. Requirements for the initiation of polyphenylalanine synthesis by recombined ribosomal subunits from yeast
- Author
-
Marleen H. Roos, Martyn H. Pranger, Henri P. J. Bloemers, and Ben van der Zeijst
- Subjects
Peptide Biosynthesis ,Poly U ,Phenylalanine ,Peptide Chain Elongation, Translational ,Saccharomyces cerevisiae ,Biology ,Ribosome ,chemistry.chemical_compound ,RNA, Transfer ,Genetics ,Peptide synthesis ,Diphtheria Toxin ,Electrophoresis, Paper ,Carbon Radioisotopes ,Peptide Chain Initiation, Translational ,Molecular Biology ,Diphtheria toxin ,Binding Sites ,General Medicine ,Ribosomal RNA ,Chromatography, Ion Exchange ,NAD ,Peptide Elongation Factors ,Yeast ,Elongation factor ,Biochemistry ,chemistry ,Puromycin ,Protein Biosynthesis ,Chromatography, Gel ,NAD+ kinase ,Transfer RNA Aminoacylation ,Fusidic Acid ,Ribosomes - Abstract
A reaction stimulated by elongation factor 2 (EF-2) is necessary for the formation of the initial peptide-bond in poly(U)-directed peptide synthesis on yeast ribosomal subunits. The stimulation is inhibited by fusidic acid or diphtheria toxin together with NAD. It is assumed that the reaction of EF-2 represents translocation: in the presence of EF-2 almost twice the amount of N-acetyl-phenylalanyl-tRNA is bound to ribosomes and moreover, upon addition of puromycin a considerable stimulation of N-acetyl-phenylalanyl-puromycin formation is found. Contradictory data in the literature on this subject may be due to nonenzymatic translocation caused by a high monovalent cation concentration in the ribosome preparations or to an unspecific method for the extraction of N-acetyl-phenylalanyl-puromycin.
- Published
- 1974